Article
Angiotensin-converting enzyme inhibitory and antioxidative activities and functional characterization of protein hydrolysates of hard-to-cook chickpeas.
Fecha
2013-08-15Autor
Medina-Godoy, Sergio
Ambriz-Pérez, DL
Fuentes-Gutiérrez, CI
Germán-Báez, LJ
Gutiérrez- Dorado, R
Reyes-Moreno, C
Valdez-Ortiz, A
Institución
Resumen
BACKGROUND:
The potential use of hard-to-cook (hardened) chickpeas to obtain value-added functional
food ingredients was evaluated. For that purpose, some nutraceutical and functional
attributes of several chickpea protein hydrolysates (CPHs) prepared from both fresh and
hard-to-cook grains were evaluated.
RESULTS:
All the CPHs prepared from both fresh and hard-to-cook grains, with the enzymes alcalase, pancreatin and papain, showed high angiotensin converting enzyme inhibitory (ACE-I) activity with IC(50) values ranging from 0.101 to 37.33 μg mL(-1) ; similarly, high levels of antioxidant activity (around 18.17-95.61 μmol Trolox equivalent antioxidant capacity μg(-1) CPH) were obtained through both the 2,2-diphenyl-1-picrylhydrazyl and 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) methods. Regarding functional characterizationof the CPHs, oil absorption values ranged from 1.91 to 2.20 mL oil g(-1) CPH, with water solubility almost 100% from pH 7 to 10.
CONCLUSION:
The high antioxidant and ACE-I activities as well as the good functional properties of the
CPH prepared from both fresh and hard-to-cook grains, suggest its use in food Formulations with value added in human health. Copyright © 2012 Society of Chemical Industry.